Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI

Sanna Askolin*, Johan P. Turkenburg, Maija Tenkanen, Sinikka Uotila, Keith S. Wilson, Merja Penttilä, Kalevi Visuri

*Corresponding author for this work

    Research output: Contribution to journalArticleScientificpeer-review

    9 Citations (Scopus)

    Abstract

    Hydrophobins are fungal proteins that are capable of altering the hydrophobicity of surfaces by self-assembly at hydrophilic-hydrophobic interfaces. Here, the growth of hydrophobin crystals suitable for X-ray crystallography is reported. The hydrophobin HFBI from Trichoderma reesei was crystallized by vapour diffusion in hanging drops in 30% PEG 4000, 0.1 M sodium citrate pH 4.3 buffer containing 0.2 M ammonium acetate and CYMAL-5 detergent (initial concentration of 2.4 mM). HFBI crystals are hexagonal and belong to space group P61 (or P65), with unit-cell parameters a = b = 45.9, c = 307.2 Å. The HFBI used in the crystallization experiments was purified from fungal cell walls.

    Original languageEnglish
    Pages (from-to)1903-1905
    Number of pages3
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume60
    Issue number10
    DOIs
    Publication statusPublished - 1 Oct 2004
    MoE publication typeA1 Journal article-refereed

    Keywords

    • hydrophobins
    • HFBI

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